Mucosal Immunology 2015
DOI: 10.1016/b978-0-12-415847-4.00019-7
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Immunoglobulin Transport and Immunoglobulin Receptors

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Cited by 17 publications
(34 citation statements)
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References 642 publications
(681 reference statements)
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“…The most primitive form of pIgR found in teleost fish contains only 2 extracellular domains, homologous to domains 1 and 5 of mammalian pIgR. Interspecies homology is greatest in domain 1, which has been shown to be critical for binding of mammalian pIgR to polymeric Igs (reviewed in [111]). Highly conserved internal disulfide bonds are found in all the Iglike domains of pIgR, characteristic of the immunoglobulin fold.…”
Section: Coevolution Of Pigr and Mucosal Igsmentioning
confidence: 99%
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“…The most primitive form of pIgR found in teleost fish contains only 2 extracellular domains, homologous to domains 1 and 5 of mammalian pIgR. Interspecies homology is greatest in domain 1, which has been shown to be critical for binding of mammalian pIgR to polymeric Igs (reviewed in [111]). Highly conserved internal disulfide bonds are found in all the Iglike domains of pIgR, characteristic of the immunoglobulin fold.…”
Section: Coevolution Of Pigr and Mucosal Igsmentioning
confidence: 99%
“…The pIgR is expressed on the surface of glandular and mucosal epithelial binds, where it binds selectively to polymeric Ig (pIg) and mediates its transport across epithelial cells into external secretions (reviewed in [17,111,112] our knowledge of pIgR-mediated transcytosis of mucosal Igs is derived from studies of mammalian secretory IgA (SIgA), as illustrated in Figure 4. Transcription of the PIGR gene and translation of pIgR mRNA is accompanied by insertion of the nascent protein into the endoplasmic reticulum.…”
Section: Unique Biological Functions Of Pigrmentioning
confidence: 99%
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